ArticleProceedings of the National Academy of Sciences of the United States of America2013
Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- Staphylococcal accessory regulator SarA-mediated modulation of autolysis and surface charge enablesmSystems · 2026Article
- Prokaryotic mechanosensitive channels mediate copper influx.Protein science : a publication of the Protein Society · 2025Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- When less is more: Counterintuitive stoichiometries and cellular abundances are essential for ABC transporters' function.Science advances · 2025Article
- The structural basis of bacterial manganese import.Science advances · 2021Article
- Assembly and Maintenance of Lipids at the Bacterial Outer Membrane.Chemical reviews · 2021Review
- Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme.Frontiers in molecular biosciences · 2021Review
- Substrate recognition and ATPase activity of theThe Journal of biological chemistry · 2020Article
- Determination of Ligand Profiles forInternational journal of molecular sciences · 2019Article
- The Different Effects of Substrates and Nucleotides on the Complex Formation of ABC Transporters.Structure (London, England : 1993) · 2019Article
- Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD.Nature chemical biology · 2018Article
- ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein.The Journal of biological chemistry · 2017Article
- Application of Proteomics for the Investigation of the Effect of Initial pH on Pathogenic Mechanisms ofFrontiers in microbiology · 2017Article
- L-glutamine Induces Expression of Listeria monocytogenes Virulence Genes.PLoS pathogens · 2017Article
- The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Scientific reports · 2016Article
- In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.The Journal of biological chemistry · 2015Article
- Real time measurements of membrane protein:receptor interactions using Surface Plasmon Resonance (SPR).Journal of visualized experiments : JoVE · 2014Article
- Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment.The Journal of biological chemistry · 2014Article
- Structural diversity of ABC transporters.The Journal of general physiology · 2014Review
- Conformational cycle of the vitamin B12 ABC importer in liposomes detected by double electron-electron resonance (DEER).The Journal of biological chemistry · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In all kingdoms of life, ATP Binding Cassette (ABC) transporters participate in many physiological and pathological processes. Despite the diversity of their functions, they have been considered to operate by a largely conserved mechanism. One deviant is the vitamin B12 transporter BtuCD that has been shown to operate by a distinct mechanism. However, it is unknown if this deviation is an exotic example, perhaps arising from the nature of the transported moiety. Here we compared two ABC importers of identical substrate specificity (molybdate/tungstate), and find that their interactions with their substrate binding proteins are utterly different. One system forms a high-affinity, slow-dissociating complex that is destabilized by nucleotide and substrate binding. The other forms a low-affinity, transient complex that is stabilized by ligands. The results highlight significant mechanistic divergence among ABC transporters, even when they share the same substrate specificity. We propose that these differences are correlated with the different folds of the transmembrane domains of ABC transporters.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.